The plus ends of growing microtubules (MTs) accumulate a diverse group of MT-associated proteins including the end-binding (EB) protein family. Like other MT plus-end tracking proteins (+TIPs), EB proteins mediate interactions between the ends of MTs, organelles, and protein complexes as well as altering MT stability. Of the three EB family members, EB3 is preferentially expressed in the CNS and is used to track MT dynamics. EB1 was shown to interact with a conserved binding site in +TIPS—namely, SxIP. EB3 is associated with cellular differentiation, and it may form a dimer with EB1 and act also in neuroprotection.
Some recent reports have shown EB3 interaction with PSD-95 at the level of the dendritic modeling and plasticity. See, e.g., Sweet et al., Bioarchitecture 2011, 1(2):69-73; Sweet et al., J. Neurosci. 2011, 31(30):1038-1047. Thus, EB3 plus-end decorated MTs control actin dynamics and regulate spine morphology and synaptic plasticity, through interaction with PSD-95, and NMDA receptor activation.